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Tumor Biology |
Vß3 and Vß5 Integrins and Promotes Cell Motility1
Department of Medicine [L. G., D. M., C. S. G., D. D. C.], Department of Microbiology, Immunology and Molecular Genetics [D. D. C.], and Department of Obstetrics and Gynecology [B. Y. K.], David Geffen School of Medicine at UCLA, Los Angeles, California 90095, Division of Gynecologic Oncology, Cedars-Sinai Medical Center, Los Angeles, California 90048 [B. Y. K.], and Gynecologic Oncology, Northwestern University, Chicago, Illinois 60611 [D. A. F.]
Periostin (PN) is a secreted protein that shares a structural homology to the axon guidance protein fasciclin I in insects. Previously, we reported that PN expression is up-regulated in epithelial ovarian tumors. We further examined the role of PN in ovarian cancer. PN is expressed in several normal tissues but not in normal ovaries and has a tendency for higher expression in fetal tissues. Ovarian cancer cells secrete PN, which can accumulate in malignant ascites of ovarian cancer patients. Purified recombinant PN supports adhesion of ovarian epithelial cells that can be inhibited by monoclonal antibodies against 
Vß3 or Vß5 integrin, but not by anti-ß1 integrin antibody. Furthermore, Vß3 integrin, but not ß1 integrins, colocalizes to the focal adhesion plaques formed on PN. Cells plated on PN form fewer stress fibers and are more motile compared with those plated on fibronectin. We propose PN functions as a ligand for Vß3 and Vß5 integrins to support adhesion and migration of ovarian epithelial cells.
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